期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：10
页码：2970-2974
DOI：10.1073/pnas.69.10.2970
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：In an attempt to gain a better understanding of the mechanism of action of carboxypeptidase A (EC 3.4.2.1 ), many kinetic studies have been undertaken using numerous substrates--both esters and peptides--that have exhibited substrate linearity, inhibition, activation, and sigmoid-shaped rate plots. Numerous interpretations of the kinetic data have been proposed, none of which are fully in accord both with kinetic data and x-ray crystallographic studies. Much of the kinetic data has been interpreted using multisite binding while the x-ray information seems to severely restrict these possibilities. We have examined the feasibility of a simple model with a single active site, without modifier sites, that allows only one substrate molecule to bind the enzyme at a time. A random-pathway model was identified that simultaneously accounts for the nonlinear kinetic data and meets the restrictions imposed by the x-ray crystallographic studies.
